Bovine plasma hydrolysates’ iron chelating capacity and its potentiating effect on ferritin synthesis in Caco-2 cells

2020 ◽  
Vol 11 (12) ◽  
pp. 10907-10912
Author(s):  
Nathalia A. Gómez-Grimaldos ◽  
Leidy J. Gómez-Sampedro ◽  
José E. Zapata-Montoya ◽  
Gabriel López-García ◽  
Antonio Cilla ◽  
...  

Bovine plasma hydrolysates with a degree of hydrolysis of 19.1% have an iron chelating capacity of 38.5 ± 0.4% and increase the synthesis of ferritin in Caco-2 cells five-fold compared to the control.

Revista EIA ◽  
2013 ◽  
Vol 9 (17) ◽  
pp. 71
Author(s):  
Omar Alfredo Figueroa ◽  
José Édgar Zapata ◽  
Gail Albeiro Gutiérrez

Se utilizó un modelo cinético para estudiar la velocidad de reacción en la hidrólisis de proteínas de plasma de bovino con alcalasa 2,4 L en un reactor batch. Se estudió la influencia de variables como la concentración inicial de sustrato y enzima sobre el grado de hidrólisis y se determinaron los parámetros cinéticos de la ecuación de velocidad, analizando su relación con las variables de trabajo. Se ajustó un modelo cinético de orden cero y desactivación enzimática por sustrato, de segundo orden, así como la relación directa entre la fracción enzima-sustrato y la tasa de formación de productos de hidrólisis.Abstract: A kinetic model was used to study the reaction rate of hydrolysis of bovine plasma proteins and alcalase 2.4 L, in a batch reactor. The influence of variables, such as the concentration of initial enzyme substrate and the degree of hydrolysis was studied, and kinetic parameters of the rate equation were determined by analyzing its relationship with the work variables. A zero-order kinetic model and enzyme deactivation by substrate was found, as well as the direct relationship between the fraction of enzyme-substrate and the rate of formation of hydrolysis products.


2019 ◽  
Vol 15 (2) ◽  
pp. 144-153 ◽  
Author(s):  
Nathalia A. Gómez ◽  
Leidy J. Gómez ◽  
José E. Zapata

Background: The animal blood that is produced in a slaughterhouse is a potential source of inexpensive proteins used in the food industry around the world. However, 60% of it is surplus, and it ends with a negative environmental impact. Introduction: The enzymatic hydrolysis of proteins represents a good way to produce peptides with different biological activities. Methods: Enzymatic hydrolysis of bovine plasma with subtilisin at an alkaline pH and 61.5°C was performed using the pH-stat method. Experiments were conducted considering the effects of a high initial substrate concentration (So) and the enzyme/substrate ratio (E/S) minimizing the processing time necessary to obtain a specific degree of hydrolysis (DH). Results: The best conditions obtained were 42 g/L of So and 0.89 AU/g substrate of E/S until a DH of 20% in 11,1 ± 1,1 min was achieved to the tested conditions, which result in a fitted empirical polynomial equation of degree 3. Conclusion: A kinetic equation is established to relate the DH and the reaction time to a relative error of less than 5% in the fit, to obtain a good antioxidant product in an industrially interesting time. Additionally, the results suggest a good adjustment of the data with a determination coefficient (R2) of 0.9745 in validation.


2020 ◽  
Vol 22 (1) ◽  
pp. 150-158
Author(s):  
Nathalia A. Gómez Grimaldos ◽  
José E.M. Zapata

Background: modern society, there is a tendency to consume products with natural origins and minimum chemical additives. This has encouraged the replacement of synthetic antioxidants for the ones obtained from natural sources, such as the antioxidants acquired from enzymatic protein hydrolysates. Objective: In this study, the process of enzymatic hydrolysis of proteins from bovine plasma, which produces hydrolysates with an Antioxidant Capacity (AC), was scaled up from 1 to 5 L. Methods: An experimental design was developed in 1 L to evaluate the effect of the Substrate concentration (So) on the time needed to reach a Degree of Hydrolysis (DH) of 20% as well as the AC. Results: The best conditions in the 1 L reactor controlled by a Titrando 842 were transferred to 5L in a BioFlo310 reactor. These conditions were achieved at a ratio of 80g/L of the substrate and 0.89 AU of Alcalase 2.4L/g of the substrate in order to obtain a level of 16.36 ± 0.21min of the 20% of DH and antioxidant capacity of 58.98 ± 1.80%. Conclusion: The results showed that DH depends significantly on So, while the antioxidant capacity only depends on the DH. Additionally, the dimensional analysis using Re as a scaling criterion allowed us to obtain the same results in the model (1 L) and the prototype (5 L).


1980 ◽  
Vol 45 (4) ◽  
pp. 1099-1108 ◽  
Author(s):  
Mikuláš Chavko ◽  
Michal Bartík ◽  
Evžen Kasafírek

A polarographic study of the hydrolysis of [8-lysine]vasopressin and some hormonogens of the vasopressin series with the blood serum of women in the last week of pregnancy was studied. The dependence of hydrolysis on pH (pH optimum: 7.4-7.50, substrate concentration (Km 1.2 . 10-5M), pH stability and thermal stability were determined. The rate of hydrolysis of individual vasopressin analogues decreases in the order: [8-lysine]vasopressin > Nα-glycyl-prolyl[8-lysine]-vasopressin > Nα-leucyl-[8-lysine]vasopressin > Nα-alanyl-[8-lysine]vasopressin > Nα-phenyl alanyl-[8-lysine]vasopressin > Nα-diglycyl-[8-lysine]vasopressin > Nα-prolyl-[8-lysine]vasopressin > Nα-triglycyl-[8-lysine]vasopressin > Nα-sarcosyl-glycyl-[8-lysine]vasopressin. The degree of hydrolysis gradually increases to a multiple with the length of the pregnancy in consequence of the presence of oxytocine. However, vasopressin is also hydrolysed to a small extent with the enzymes from the blood sera of non-pregnant women. Under similar analytical conditions oxytocin was not hydrolysed with the sera of non-pregnant women and therefore oxytocin is a more suitable substrate than vasopressin for polarographic determination of serum oxytocinase.


2004 ◽  
Vol 127 (5) ◽  
pp. 598-603 ◽  
Author(s):  
Anna Gallí ◽  
Gaetano Bergamaschi ◽  
Helios Recalde ◽  
Giorgio Biasiotto ◽  
Paolo Santambrogio ◽  
...  

2013 ◽  
Vol 411-414 ◽  
pp. 3205-3209
Author(s):  
Fang Qian ◽  
Lei Zhao ◽  
Shu Juan Jiang ◽  
Guang Qing Mu

Based on single factor analysis for the enzymatic hydrolysis of whey protein, papain was selected as the optimal enzyme and its enzymatic hydrolysis conditions were optimized by the quadratic regression orthogonal rotary test. The orthogonal regression model for degree of hydrolysis (DH) to three factors including temperature (X1), time (X2), enzyme dosage (X3) was established as follow: DH=10.40+0.22X1+0.30X2+1.31X3+0.019X1X2+0.011X1X3-0.039X2X3-0.39X12-0.16X22-0.40X32, Verification test showed a DH of 11.7% was obtained at the optimal hydrolysis condition of 56.6°C, 113.8 min and enzyme 8213.7 U /g protein, which basically consisted with the model theoretical value.


2010 ◽  
Vol 2010 ◽  
pp. 1-5 ◽  
Author(s):  
Margarita D. Marinova ◽  
Bozhidar P. Tchorbanov

Enzymatic hydrolysates of honeybee-collected pollen were prepared using food-grade proteinase and aminopeptidases entirely of plant origin. Bromelain from pineapple stem was applied (8 mAU/g substrate) in the first hydrolysis stage. Aminopeptidase (0.05 U/g substrate) and proline iminopeptidase (0.03 U/g substrate) from cabbage leaves (Brassica oleracea var. capitata), and aminopeptidase (0.2 U/g substrate) from chick-pea cotyledons (Cicer arietinum L.) were involved in the additional hydrolysis of the peptide mixtures. The degree of hydrolysis (DH), total phenolic contents, and protein contents of these hydrolysates were as follows: DH (about 20–28%), total phenolics (15.3–27.2 μg/mg sample powder), and proteins (162.7–242.8 μg/mg sample powder), respectively. The hydrolysates possessed high antiradical scavenging activity determined with DPPH (42–46% inhibition). The prepared hydrolysates of bee-collected flower pollen may be regarded as effective natural and functional dietary food supplements due to their remarkable content of polyphenol substances and significant radical-scavenging capacity with special regard to their nutritional-physiological implications.


1922 ◽  
Vol 5 (2) ◽  
pp. 181-188 ◽  
Author(s):  
M. H. Jacobs

1. It may be shown by means of cells of the flowers of a hybrid Rhododendron which contain a natural indicator, by means of starfish eggs stained with neutral red, and by means of an "artificial cell" in which living frog's skin is employed that increased intracellular alkalinity may be brought about by solutions of a decidedly acid reaction which contain ammonium salts. 2. These results are analogous to those previously obtained with the CO2-bicarbonate system, and depend on the facts: (a) that NH4OH is sufficiently weak as a base to permit a certain degree of hydrolysis of its salts; and (b) that living cells are freely permeable to NH4OH (or NH3?) and not to mineral and many organic acids, and presumably not at least to the same extent to ammonium salts as such.


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